Chemical synthesis and evaluation of a backbone-cyclized minimized 2-helix Z-domain
2011 (English)In: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 17, no 6, 463-469 p.Article in journal (Refereed) Published
The Z-molecule is a small, engineered IgG-binding affinity protein derived from the immunoglobulin-binding domain B of Staphylococcus aureus protein A. The Z-domain consists of 58 amino acids forming a well-defined antiparallel three-helix structure. Two of the three helices are involved in ligand binding, whereas the third helix provides structural support to the three-helix bundle. The small size and the stable three-helix structure are two attractive properties comprised in the Z-domain, but a further reduction in size of the protein is valuable for several reasons. Reduction in size facilitates synthetic production of any protein-based molecule, which is beneficial from an economical viewpoint. In addition, a smaller protein is easier to manipulate through chemical modifications. By omitting the third stabilizing helix from the Z-domain and joining the N- and C-termini by a native peptide bond, the affinity protein obtains the advantageous properties of a smaller scaffold and in addition becomes resistant to exoproteases. We here demonstrate the synthesis and evaluation of a novel cyclic two-helix Z-domain. The molecule has retained affinity for its target protein, is resistant to heat treatment, and lacks both N- and C-termini. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.
Place, publisher, year, edition, pages
2011. Vol. 17, no 6, 463-469 p.
protein scaffold, Z-domain, two-helix protein, SPPS, IgG, affinity purification
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:kth:diva-34212DOI: 10.1002/psc.1346ISI: 000290633700007ScopusID: 2-s2.0-79955908750OAI: oai:DiVA.org:kth-34212DiVA: diva2:423486
QC 201106152011-06-152011-05-302011-06-15Bibliographically approved